Isolation of bovine seminal ribonuclease by affinity chromatography

Krietsch, Wolfgang K. G.; Simm, Franz C.; Hertenberger, B; Kuntz, Günter W. K.; Wächter, Elmar

doi:10.1016/0003-2697(83)90366-4

Cited by 8 publications

(1 citation statement)

References 14 publications

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“…Seminal (2) and milk (3) RNases have also been found. Several Nobel prizes have been awarded to work on RNases, signifying the importance of RNases.…”

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confidence: 94%

Isolation of a Novel Thermolabile Heterodimeric Ribonuclease with Antifungal and Antiproliferative Activities from Roots of the Sanchi Ginseng Panax notoginseng

Lam

2001

Biochemical and Biophysical Research Communications

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“…Seminal (2) and milk (3) RNases have also been found. Several Nobel prizes have been awarded to work on RNases, signifying the importance of RNases.…”

mentioning

confidence: 94%

Isolation of a Novel Thermolabile Heterodimeric Ribonuclease with Antifungal and Antiproliferative Activities from Roots of the Sanchi Ginseng Panax notoginseng

Lam

2001

Biochemical and Biophysical Research Communications

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Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases

Beintema

Laan

1986

FEBS Letters

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There are 33 invariant amino acid positions out of 132 positions in 42 ~nv~st~~ated sequences of ribonucfeases from a number of mammalian species and a reptile (snapping turtle, Chetydrcr serpentina). These invariant residues are nnequafly distributed over 3 different parts of the mofeculle, The bbe of the S-protein part of the mole&e, which lacks one disulfide bridge and has two shortened loops in turtle ribotruclease, has the lowest percentage of invariant residues, although the active-site residue His I19 is Iocated in this part.Pancre&ic tibonucleases form a group of homologous proteins present in considerable quantities in the pancreas of a number of mammalian taxa and a few reptiles [ 1,2], An extensive study on the molecular evolution of pancreatic ribon&eases included many mammalian species, but no reptiles [3f. Recently the amino acid sequence of snapping turtle (Cfaeiydra serpPntina) ribonuclease has been determined 141. This sequence shows a number of structural variations not observed in the mammalian sequences determined hitherto, In addition, there are differences in enzymic properties [4]. Nere the amino acid sequence of turtle ribonuclease is discussed in relation with likely similarities and dissimilarities of its nonformation with that of bovine ribon~~lease [5-71.The amino acid sequence of snapping turtle ribanuclease, with the residues numbered both continuously from the N-to C-terminus and according to the bovine ribonu~lease numbering, is given in fig.la. The polypeptide chain of turtle ribonuctease consists of 113 amino acid residues. Compared to most ribonu~leases, the N-terminal residue, 3 residues in the loop near residue 71 and 2 residues in the loop near residue 114 are deleted, and there is one additional residue in the loop near residue 23. The half-cystines at positions 65 and 72, which form a disulfide bond in mammalian ribonucleases, are not present in turtle ribonuckase.The results of the prediction of secondarystructural elements in the amino acid sequence of turtle ribonuclease are summarized in fig. 1

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